View in EDS

Novel Leech Antimicrobial Peptides, Hirunipins: Real‐Time 3D Monitoring of Antimicrobial and Antibiofilm Mechanisms Using Optical Diffraction Tomography.

Saved in:
Bibliographic Details
Title: Novel Leech Antimicrobial Peptides, Hirunipins: Real‐Time 3D Monitoring of Antimicrobial and Antibiofilm Mechanisms Using Optical Diffraction Tomography.
Authors: Kumar, S. Dinesh, Park, Jeongwon, Radhakrishnan, Naveen Kumar, Aryal, Yam Prasad, Jeong, Geon‐Hwi, Pyo, In‐Hyeok, Ganbaatar, Byambasuren, Lee, Chul Won, Yang, Sungtae, Shin, Younhee, Subramaniyam, Sathiyamoorthy, Lim, Yu‐jin, Kim, Sung‐Hak, Lee, Seongsoo, Shin, Song Yub, Cho, Sung‐Jin
Source: Advanced Science; 3/13/2025, Vol. 12 Issue 10, p1-17, 17p
Subject Terms: ANTIMICROBIAL peptides, OPTICAL tomography, MEMBRANE permeability (Technology), OPTICAL diffraction, BACTERIAL cell walls
Abstract: Antimicrobial peptides (AMPs) are promising agents for treating antibiotic‐resistant bacterial infections. Although discovering novel AMPs is crucial for combating multidrug‐resistant bacteria and biofilm‐related infections, their clinical potential relies on precise, real‐time evaluation of efficacy, toxicity, and mechanisms. Optical diffraction tomography (ODT), a label‐free imaging technology, enables real‐time visualization of bacterial morphological changes, membrane damage, and biofilm formation over time. Here, a computational analysis of the leech transcriptome using an advanced AI‐based peptide screening strategy with ODT to identify potential AMPs is employed. Among the 19 potential AMPs identified, hirunipin 2 demonstrates potent antibacterial activity, low mammalian cytotoxicity, and minimal hemolytic effects. It demonstrates efficacy comparable to melittin, resistance to physiological salts and human serum, and a low likelihood of inducing bacterial resistance. Microscopy and 3D‐ODT confirm its disruption of bacterial membranes and intracellular aggregation, leading to cell death. Notably, hirunipin 2 effectively inhibits biofilm formation, eradicates preformed biofilms, and synergizes with antibiotics against multidrug‐resistant Acinetobacter baumannii (MDRAB) by enhancing membrane permeability. Additionally, hirunipin 2 significantly suppresses pro‐inflammatory cytokine expression in LPS‐stimulated macrophages, highlighting its anti‐inflammatory properties. These findings highlight hirunipin 2 as a strong candidate for developing novel antibacterial, anti‐inflammatory, and antibiofilm therapies, particularly against multidrug‐resistant bacterial infections. [ABSTRACT FROM AUTHOR]
Copyright of Advanced Science is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Complementary Index
Description
Abstract:Antimicrobial peptides (AMPs) are promising agents for treating antibiotic‐resistant bacterial infections. Although discovering novel AMPs is crucial for combating multidrug‐resistant bacteria and biofilm‐related infections, their clinical potential relies on precise, real‐time evaluation of efficacy, toxicity, and mechanisms. Optical diffraction tomography (ODT), a label‐free imaging technology, enables real‐time visualization of bacterial morphological changes, membrane damage, and biofilm formation over time. Here, a computational analysis of the leech transcriptome using an advanced AI‐based peptide screening strategy with ODT to identify potential AMPs is employed. Among the 19 potential AMPs identified, hirunipin 2 demonstrates potent antibacterial activity, low mammalian cytotoxicity, and minimal hemolytic effects. It demonstrates efficacy comparable to melittin, resistance to physiological salts and human serum, and a low likelihood of inducing bacterial resistance. Microscopy and 3D‐ODT confirm its disruption of bacterial membranes and intracellular aggregation, leading to cell death. Notably, hirunipin 2 effectively inhibits biofilm formation, eradicates preformed biofilms, and synergizes with antibiotics against multidrug‐resistant Acinetobacter baumannii (MDRAB) by enhancing membrane permeability. Additionally, hirunipin 2 significantly suppresses pro‐inflammatory cytokine expression in LPS‐stimulated macrophages, highlighting its anti‐inflammatory properties. These findings highlight hirunipin 2 as a strong candidate for developing novel antibacterial, anti‐inflammatory, and antibiofilm therapies, particularly against multidrug‐resistant bacterial infections. [ABSTRACT FROM AUTHOR]
ISSN:21983844
DOI:10.1002/advs.202409803